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Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed

Morgunova, Ekaterina ; Tuuttila, Ari ; Bergmann, Ulrich ; Isupov, Mikhail ; Lindqvist, Ylva ; Schneider, Gunter ; Tryggvason, Karl

Science (American Association for the Advancement of Science), 1999-06, Vol.284 (5420), p.1667-1670 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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Título:
Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed
Autor: Morgunova, Ekaterina ; Tuuttila, Ari ; Bergmann, Ulrich ; Isupov, Mikhail ; Lindqvist, Ylva ; Schneider, Gunter ; Tryggvason, Karl
Assuntos: Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Atoms ; Biochemistry ; Biological and medical sciences ; Catalytic Domain ; Connective tissues ; Crystals ; Diseases ; Enzyme Activation ; Enzyme Precursors - chemistry ; Enzyme Precursors - metabolism ; Enzymes ; Enzymes and enzyme inhibitors ; Fibronectins - chemistry ; Fundamental and applied biological sciences. Psychology ; Gelatinases - chemistry ; Gelatinases - metabolism ; Gelatins ; Hemopexin - chemistry ; Humans ; Hydrogen Bonding ; Hydrogen bonds ; Hydrolases ; Literary Devices ; Matrix mechanics ; Matrix Metalloproteinase 2 ; Medicin och hälsovetenskap ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - metabolism ; Metalloenzymes ; Models, Molecular ; Molecular Sequence Data ; Molecules ; Peptides ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins ; Stromal cells ; Tumors
É parte de: Science (American Association for the Advancement of Science), 1999-06, Vol.284 (5420), p.1667-1670
Notas: ObjectType-Article-2
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Descrição: Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.
Editor: Washington, DC: American Society for the Advancement of Science
Idioma: Inglês

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Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed

Morgunova, Ekaterina ; Tuuttila, Ari ; Bergmann, Ulrich ; Isupov, Mikhail ; Lindqvist, Ylva ; Schneider, Gunter ; Tryggvason, Karl

Washington, DC: American Society for the Advancement of Science

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